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J Biol Chem, Vol. 273, Issue 24, 14819-14826, June 12, 1998
From the The membrane-spanning protein, band 3, anchors
the spectrin-based membrane skeleton to the lipid bilayer via the
bridging protein, ankyrin. To understand how band 3 subunit
stoichiometry influences this membrane-skeletal junction, we have
induced changes in the band 3 association equilibrium and assayed the
kinetics and equilibrium properties of ankyrin binding. We observe that band 3 oligomers convert slowly to dimers and ultimately monomers following removal of ankyrin. Addition of excess ankyrin back to these
membranes enriched in dissociated band 3 then shifts band 3 almost
entirely to tetramers, confirming that the tetrameric form of band 3 constitutes the preferred oligomeric state of ankyrin binding.
4,4'-Diisothiocyanostilbene-2,2'-disulfonic acid (DIDS) labeling of band 3, which is shown to shift most of the band 3 population to dimers, eliminates the majority of ankyrin-binding sites
on the membrane and greatly reduces retention of band 3 in
detergent-extracted membrane skeletons. Furthermore,
DIDS
Effect of Band 3 Subunit Equilibrium on the Kinetics and
Affinity of Ankyrin Binding to Erythrocyte Membrane Vesicles
,, and
Department of Chemistry, Purdue University,
West Lafayette, Indiana 47907-1393
modified membranes lack all low affinity
ankyrin-binding sites and roughly half of all high affinity sites.
Since labeled membranes lack the rapid kinetic phase of ankyrin binding
and exhibit only half of the normal amplitude of the slow kinetic
phase, it can be concluded that the rapid phase of ankyrin association
involves low affinity sites and the slow phase involves high affinity
sites. A model accounting for these data and most previous data on
ankyrin-band 3 interactions is provided.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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